ID C5FNQ8_ARTOC Unreviewed; 676 AA.
AC C5FNQ8;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Heat shock protein SSC1 {ECO:0000313|EMBL:EEQ31761.1};
GN ORFNames=MCYG_04580 {ECO:0000313|EMBL:EEQ31761.1};
OS Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Microsporum.
OX NCBI_TaxID=554155 {ECO:0000313|EMBL:EEQ31761.1, ECO:0000313|Proteomes:UP000002035};
RN [1] {ECO:0000313|Proteomes:UP000002035}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4605 / CBS 113480 {ECO:0000313|Proteomes:UP000002035};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000256|RuleBase:RU003322}.
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DR EMBL; DS995704; EEQ31761.1; -; Genomic_DNA.
DR RefSeq; XP_002846843.1; XM_002846797.1.
DR AlphaFoldDB; C5FNQ8; -.
DR STRING; 554155.C5FNQ8; -.
DR GeneID; 9229958; -.
DR VEuPathDB; FungiDB:MCYG_04580; -.
DR eggNOG; KOG0102; Eukaryota.
DR HOGENOM; CLU_005965_2_1_1; -.
DR OMA; MGTDWKI; -.
DR OrthoDB; 143at2759; -.
DR Proteomes; UP000002035; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR CDD; cd11733; HSPA9-like_NBD; 1.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 3.30.420.40; -; 2.
DR HAMAP; MF_00332; DnaK; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR012725; Chaperone_DnaK.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR029048; HSP70_C_sf.
DR InterPro; IPR029047; HSP70_peptide-bd_sf.
DR InterPro; IPR013126; Hsp_70_fam.
DR NCBIfam; TIGR02350; prok_dnaK; 1.
DR PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR PANTHER; PTHR19375:SF184; STRESS-70 PROTEIN, MITOCHONDRIAL; 1.
DR Pfam; PF00012; HSP70; 1.
DR PRINTS; PR00301; HEATSHOCK70.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 1.
DR PROSITE; PS00297; HSP70_1; 1.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003322};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU003322};
KW Reference proteome {ECO:0000313|Proteomes:UP000002035};
KW Stress response {ECO:0000313|EMBL:EEQ31761.1}.
FT REGION 644..676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 574..601
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 676 AA; 73421 MW; ABF807747D40DD10 CRC64;
MIASRICRAA PRVPTQFIRS PAFRAPSIPF RRWNSTEGGE EKVKGQVIGI DLGTTNSAVA
VMEGKTPKIM ENSEGTRTTP SVVAFTKDGE RLVGVAAKRQ AVVNPENTLF ATKRLIGRKF
TDPECQRDLS EVPYKIIQHT NGDAWVEAQG QKYSPSQIGG FILQKMKETA EGYLNKPIKN
GVVTVPAYFN DSQRQATKDA GQIAGLNVLR VVNEPTAAAL AYGLEKEQDR VIAVYDLGGG
TFDISILEIQ KGVFEVKSTN GDTHLGGEDF DITLVRNIVQ QFKKESGLDL SGDRMAIQRI
REAAEKAKIE LSSASQTEIN LPFITADASG AKHINSKLSR SQLEALVDPL IQRTVEPVRK
ALKDANLTAK DIQEVILVGG MTRMPKVTES VKSIFGREPA KSVNPDEAVA IGAAIQGAVL
AGEVTDVLLL DVTPLSLGIE TLGGVFTRLI NRNTTIPTKK SQTFSTAADF QTAVEIKVYQ
GERELVRDNK LLGNFQLVGI PPAHRGVPQI EVTFDIDADS IVHVHAKDKS TNKDQSITIA
SGSGLSDTEI QNMVNDAETY RAQDIERKAI IEGANRADSV LNDTEKALKE FEDKLDKAEA
TQISEKIAAL REVVAKCQSG ESTLSAEELK AKVDDLQTSS LTLFDKMHKA RHEESQQQQP
QGGADAPPAG EGEKKQ
//
